Evidence map›Paper›PMID 41493814›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2026

Hydroxo-bridged active site of flavodiiron NO reductase revealed by NRVS and DFT.

Filipe Folgosa, Vladimir Pelmenschikov, Giorgio Caserta, Matthias Keck, Christian Lorent, Konstantin Laun, Yoshitaka Yoda, Leland B Gee, Martin Kaupp, Kenji Tamasaku and 5 more

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

2 citing papers in PubMed.

  1. Article
  2. Hydroxo-bridged active site of flavodiiron NO reductase revealed by NRVS and DFT.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

15 authors.

Filipe Folgosa *Instituto de Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa, Oeiras 2780-157, Portugal.ORCID 0000-0001-5879-151X
Vladimir Pelmenschikov *Institut für Chemie, Technische Universität Berlin, Berlin 10623, Germany.ORCID 0000-0002-0523-4418
Giorgio Caserta *Institut für Chemie, Technische Universität Berlin, Berlin 10623, Germany.ORCID 0000-0003-0986-3059
Matthias KeckDepartment of Chemistry, Humboldt-Universität zu Berlin, Berlin 12489, Germany.
Christian LorentInstitut für Chemie, Technische Universität Berlin, Berlin 10623, Germany.
Konstantin LaunInstitut für Chemie, Technische Universität Berlin, Berlin 10623, Germany.
Yoshitaka YodaPrecision Spectroscopy Division, SPring-8/JASRI, Sayo 679-5198, Japan.
Leland B GeeSLAC National Accelerator Laboratory, Menlo Park, CA 94025s.ORCID 0000-0002-5817-3997
Martin KauppInstitut für Chemie, Technische Universität Berlin, Berlin 10623, Germany.ORCID 0000-0003-1582-2819
Kenji TamasakuPrecision Spectroscopy Division, SPring-8/JASRI, Sayo 679-5198, Japan.ORCID 0000-0003-1440-0518
James A BirrellSchool of Life Science, University of Essex, Colchester CO4 3SQ, United Kingdom.ORCID 0000-0002-0939-0573
Ilya SergueevDeutsches Elektronen-Synchrotron, Hamburg 22607, Germany.ORCID 0000-0002-7614-2238
Christian LimbergDepartment of Chemistry, Humboldt-Universität zu Berlin, Berlin 12489, Germany.ORCID 0000-0002-0751-1386
Miguel TeixeiraInstituto de Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa, Oeiras 2780-157, Portugal.
Lars LauterbachInstitute of Applied Microbiology, Rheinisch-Westfälische Technische Hochschule (RWTH) Aachen University, Aachen 52074, Germany.ORCID 0000-0002-6601-6473

Funding

Deutsche Forschungsgemeinschaft (DFG) EXC 2186 - 390919832 EXC 2008 - 390540038 SPP 1927) Project BI 2198/1-1Fundação para a Ciência e a Tecnologia PTDC/BIA-BQM/0562/2020LS4FUTURE Associated Laboratory LA/P/0087/2020MOSTMICRO-ITQB R&D Unit UIDB/04612/2020
6 · The paper itself

Abstract

The use of oxygen and nitrate as terminal electron acceptors provides organisms with a huge amount of available energy but necessitates methods to detoxify reactive intermediates. The mechanisms of NO and O

Indexed as

Escherichia coli ProteinsOxidoreductasesCatalytic DomainCrystallography, X-RayDensity Functional TheoryEscherichia coliIronLigandsModels, MolecularOxidation-ReductionSpectroscopy, MossbauerEscherichia coli ProteinsIronLigandsnitric-oxide reductaseOxidoreductasesDFTdiiron enzymesNO reductionNRVSreaction mechanism

Identifiers

PMID41493814
PMCPMC12799149

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.